3c52 | pdb_00003c52

Class II fructose-1,6-bisphosphate aldolase from helicobacter pylori in complex with phosphoglycolohydroxamic acid, a competitive inhibitor

spinqualitylabelsall models 3c52, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3c52 is a 2 chain structure with sequence from Atcc 43504. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, NA, PGH, ZN Related: 3c3s, 3c56 Gene: fba (ATCC 43504) Activity: Fructose-bisphosphate aldolase, with EC number 4.1.2.13 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ALF_HELPY] Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed We report the synthesis and biochemical evaluation of selective inhibitors of class II (zinc-dependent) fructose bisphosphate aldolases. The most active compound is a simplified analogue of fructose bisphosphate, bearing a well-positioned metal chelating group. It is a powerful and highly selective competitive inhibitor of isolated class II aldolases. We report crystallographic studies of this inhibitor bound in the active site of the Helicobacter pylori enzyme. The compound also shows activity against Mycobacterium tuberculosis isolates. Synthesis and Biochemical Evaluation of Selective Inhibitors of Class II Fructose Bisphosphate Aldolases: Towards New Synthetic Antibiotics.,Fonvielle M, Coincon M, Daher R, Desbenoit N, Kosieradzka K, Barilone N, Gicquel B, Sygusch J, Jackson M, Therisod M Chemistry. 2008 Aug 7. PMID:18688832 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aldolase

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